Cell Structure: Plasma Membrane City Part: City Wall/Boundary

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The Cell City Cell Structure: Plasma Membrane City Part: City Wall/Boundary • Flexible, selectively permeable boundary that helps control what enters and leaves the cell Cell Structure: Cytoplasm City Part: Lakes, Streams & Rivers • Semi-fluid material that organelles float in Cell Structure: Cytoskeleton City Part: Foundations • Supporting network of long thin protein fibers that form a framework for the cell • Provides an anchor for the organelles inside the cell Cell Structure: Nucleus City Part: Mayor’s Office/City Hall • Directs all cell processes • Contains cell’s DNA • Center: Nucleolus (makes ribosomes) Cell Structure: Ribosome City Part: Factory • Manufactures proteins • Made of RNA & protein Cell Structure: Endoplasmic Reticulum City Part: Highway/Road System • Responsible for production of proteins and lipids • Transports materials • Rough E.R.: contains ribosomes • Smooth E.R.: no ribosomes Cell Structure: Golgi Apparatus City Part: Post Office • Modifies, sorts, and packages proteins into sacs called vesicles Cell Structure: Vacuole City Part: Storage Units • Sac used to store food, enzymes, and other materials within the cytoplasm Cell Structure: Lysosome City Part: Garbage Company • Digests worn-out or extra organelles and food particles Cell Structure: Centrioles City Part: City Blocks • Made of microtubules • Aids in cell division Cell Structure: Mitochondria City Part: Power Plant • Generates energy for the cell • Converts fuel particles into usable energy Cell Structure: Chloroplast City Part: Solar Power Plant • Captures light energy and converts it into chemical energy through a process known as photosynthesis • Plant cells only Cell Structure: Cilia & Flagella City Part: Taxi/Bus Service • Aids in movement of the cell • Cilia: short, hair-like projections • Flagella: long, moves with a whiplike motion.

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Common Features of All Cells Bacterial
www.denniskunkel.com Tour of the Cell part 1 Today’s Topics • Finish Nucleic Acids Cells • Properties of all cells – Prokaryotes and Eukaryotes • Functions of Major Cellular Organelles – Information – Synthesis&Transport – Energy Conversion – Recycling – Structure and Movement Bacterial cell Animal Cell 9/12/12 (Prokaryote) (Eukaryote) 2 www.denniskunkel.com Common features of all cells • Plasma Membrane – defines inside from outside • Cytosol – Semifluid “inside” of the cell • DNA “chromosomes” - Genetic material – hereditary instructions • Ribosomes – “factories” to synthesize proteins 4 Plasma membrane Bacterial (Prokaryotic) Cell Ribosomes! Plasma membrane! Bacterial Cell wall! chromosome ! Phospholipid bilayer Proteins 0.5 !m! Flagella! No internal membranes 5 6 1 Figure 6.2b 1 cm Eukaryotic Cell Frog egg 1 mm Human egg 100 µm Most plant and animal cells 10 m µ Nucleus Most bacteria Light microscopy Mitochondrion 1 µm Super- 100 nm Smallest bacteria Viruses resolution microscopy Ribosomes 10 nm Electron microscopy Proteins Lipids 1 nm Small molecules Contains internal organelles 7 0.1 nm Atoms endoplasmicENDOPLASMIC RETICULUM reticulum (ER) ENDOPLASMIC RETICULUM (ER) NUCLEUS NUCLEUS Rough ER Smooth ER nucleus Rough ER Smooth ER Nucleus Plasma membrane Plasma membrane Centrosome Centrosome cytoskeletonCYTOSKELETON CYTOSKELETON Microfilaments You should Microfilaments Intermediate filaments know everything Intermediate filaments Microtubules in Fig 6.9 ribosomesRibosomes Microtubules Ribosomes cytosol GolgiGolgi apparatus apparatus Golgi apparatus Peroxisome Peroxisome In animal cells but not plant cells: In animal cells but not plant cells: Lysosome Lysosomes Lysosome Lysosomes Figure 6.9 Centrioles Figure 6.9 Centrioles Mitochondrion lysosome Flagella (in some plant 9sperm) Mitochondrion Flagella (in some plant10 sperm) mitochondrion Nuclear envelope Nucleus Nucleus 1 !m Nucleolus Chromatin Nuclear envelope: Inner membrane Outer membrane Pores Pore complex Rough ER Surface of nuclear envelope.
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Evidence for an Alternate Pathway for Lysosomal Enzyme Targeting (Oligosaccharides/Lysosomes/Phosphorylation) CHRISTOPHER A
Proc. NatL Acad. Sci. USA Vol. 80, pp. 775-779, February 1983 Cell Biology Identification and characterization of cells deficient in the mannose 6-phosphate receptor: Evidence for an alternate pathway for lysosomal enzyme targeting (oligosaccharides/lysosomes/phosphorylation) CHRISTOPHER A. GABEL, DANIEL E. GOLDBERG, AND STUART KORNFELD Departments of Internal Medicine and Biological Chemistry, Division of Hematology-Oncology, Washington University School of Medicine, St. Louis, Missouri 63110 Contributed by Stuart Kornfeld, November 3, 1982 ABSTRACT Newly synthesized lysosomal enzymes acquire dence that this cell line is deficient in Man-6-P receptor activity. phosphomannosyl units, which allow bindingofthe enzymes to the We also identify several additional cell lines that lack receptor mannose 6-phosphate receptor and subsequent translocation to activity yet possess high levels ofintracellular hydrolase activity. lysosomes. In some cell types, this sequence ofevents is necessary These data indicate that some cells possess pathways indepen- for the delivery ofthese enzymes to lysosomes. Using a slime mold dent of the Man-6-P receptor for the intracellular transport of lysosomal hydrolase as a probe, we have identified three murine acid hydrolases to lysosomes. cell lines that lack the receptor and one line that contains very low (3%) receptor activity. Each ofthese lines synthesizes the mannose MATERIALS AND METHODS 6-phosphate recognition marker on its lysosomal enzymes, but, Cells. BW5147 mouse lymphoma, P388D1 mouse macro- unlike cell lines with high levels of receptor, the cells accumulate MOPC 315 oligosaccharides containing phosphomonoesters. The receptor- phage, J774.2 mouse macrophage, mouse L cells, deficient lines possess high levels of intracellular acid hydrolase mouse myeloma, Chinese hamster ovary (CHO), and (human) activity, which is contained in dense granules characteristic of ly- HeLa cells were grown in suspension culture in a minimal es- sosomes.
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The Endomembrane System and Proteins
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A Mitochondria–Lysosome Transport Pathway
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Written Response #5
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The Splicing Factor XAB2 Interacts with ERCC1-XPF and XPG for RNA-Loop Processing During Mammalian Development
bioRxiv preprint doi: https://doi.org/10.1101/2020.07.20.211441; this version posted July 21, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. The Splicing Factor XAB2 interacts with ERCC1-XPF and XPG for RNA-loop processing during mammalian development Evi Goulielmaki1*, Maria Tsekrekou1,2*, Nikos Batsiotos1,2, Mariana Ascensão-Ferreira3, Eleftheria Ledaki1, Kalliopi Stratigi1, Georgia Chatzinikolaou1, Pantelis Topalis1, Theodore Kosteas1, Janine Altmüller4, Jeroen A. Demmers5, Nuno L. Barbosa-Morais3, George A. Garinis1,2* 1. Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology- Hellas, GR70013, Heraklion, Crete, Greece, 2. Department of Biology, University of Crete, Heraklion, Crete, Greece, 3. Instituto de Medicina Molecular João Lobo Antunes, Faculdade de Medicina da Universidade de Lisboa, Avenida Professor Egas Moniz, 1649-028 Lisboa, Portugal, 4. Cologne Center for Genomics (CCG), Institute for Genetics, University of Cologne, 50931, Cologne, Germany, 5. Proteomics Center, Netherlands Proteomics Center, and Department of Biochemistry, Erasmus University Medical Center, the Netherlands. Corresponding author: George A. Garinis ([email protected]) *: equally contributing authors bioRxiv preprint doi: https://doi.org/10.1101/2020.07.20.211441; this version posted July 21, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Abstract RNA splicing, transcription and the DNA damage response are intriguingly linked in mammals but the underlying mechanisms remain poorly understood. Using an in vivo biotinylation tagging approach in mice, we show that the splicing factor XAB2 interacts with the core spliceosome and that it binds to spliceosomal U4 and U6 snRNAs and pre-mRNAs in developing livers.
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Studies on the Mechanisms of Autophagy: Formation of the Autophagic Vacuole W
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A Physicochemical Perspective of Aging from Single-Cell Analysis Of
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Reflux of Endoplasmic Reticulum Proteins to the Cytosol Yields Inactivation of Tumor Suppressors
bioRxiv preprint doi: https://doi.org/10.1101/2020.04.13.038935; this version posted April 13, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Reflux of Endoplasmic Reticulum proteins to the cytosol yields inactivation of tumor suppressors Daria Sicari1,2, Raphael Pineau1,2, Pierre-Jean Le Reste1,2,3, Luc Negroni4,5,6,7, Sophie Chat8, Aiman Mohtar9, Daniel Thomas8, Reynald Gillet8, M. Ted Hupp9,10, Eric Chevet1,2* and Aeid Igbaria1,2,11* 1Inserm U1242, University of Rennes, Rennes, France. 2Centre de lutte contre le cancer Eugène Marquis, Rennes, France. 3Neurosurgery Dept, University Hospital of Rennes, 35000 Rennes, France. 4Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France. 5Centre National de la Recherche Scientifique, UMR7104, 67404 Illkirch, France. 6Institut National de la Santé et de la Recherche Médicale, U1258, 67404 Illkirch, France. 7Université de Strasbourg, 67404 Illkirch, France. 8Univ. Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France. 9Edinburgh Cancer Research Centre at the Institute of Genetics and Molecular Medicine, Edinburgh University, Edinburgh, UK. 10International Centre for Cancer Vaccine Science, Gdansk, Poland. 11Department of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva 8410501, Israel. *Correspondence: [email protected], or [email protected] ABSTRACT: In the past decades many studies reported Endoplasmic Reticulum (ER) resident proteins to localize to the cytosol but the mechanisms by which this occurs and whether these proteins exert cytosolic functions remain unknown. We found that select ER luminal proteins accumulate in the cytosol of glioblastoma cells isolated from mouse and human tumors.
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Nucleolus: a Central Hub for Nuclear Functions Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, Sergey Razin, Yegor Vassetzky
Nucleolus: A Central Hub for Nuclear Functions Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, Sergey Razin, Yegor Vassetzky To cite this version: Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, et al.. Nucleolus: A Central Hub for Nuclear Functions. Trends in Cell Biology, Elsevier, 2019, 29 (8), pp.647-659. 10.1016/j.tcb.2019.04.003. hal-02322927 HAL Id: hal-02322927 https://hal.archives-ouvertes.fr/hal-02322927 Submitted on 18 Nov 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Nucleolus: A Central Hub for Nuclear Functions Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, Sergey Razin, Yegor Vassetzky To cite this version: Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, et al.. Nucleolus: A Central Hub for Nuclear Functions. Trends in Cell Biology, Elsevier, 2019, 29 (8), pp.647-659. 10.1016/j.tcb.2019.04.003. hal-02322927 HAL Id: hal-02322927 https://hal.archives-ouvertes.fr/hal-02322927 Submitted on 18 Nov 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not.
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